Q9V1J0 (LEUC2_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
3-isopropylmalate dehydratase large subunit 2
EC=4.2.1.33

Alternative name(s):
Alpha-IPM isomerase 2
Short name=IPMI 2
Isopropylmalate isomerase 2

Gene names

Name:	leuC2
Ordered Locus Names:	PYRAB04370
ORF Names:	PAB0287

Organism

Pyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]

Taxonomic identifier

272844 [NCBI]

Taxonomic lineage

Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length	380 AA.
Sequence status	Complete.
Protein existence	Inferred from homology

General annotation (Comments)

Function	Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate. HAMAP MF_01027
Catalytic activity	(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmaleate + H2O. HAMAP MF_01027 (2S)-2-isopropylmaleate + H2O = (2S)-2-isopropylmalate. HAMAP MF_01027
Cofactor	Binds 1 4Fe-4S cluster per subunit By similarity. HAMAP MF_01027
Pathway	Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4. HAMAP MF_01027
Subunit structure	Heterodimer of LeuC and LeuD By similarity. HAMAP MF_01027
Sequence similarities	Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Branched-chain amino acid biosynthesis Leucine biosynthesis
Ligand	4Fe-4S Iron Iron-sulfur Metal-binding
Molecular function	Lyase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	leucine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	3-isopropylmalate dehydratase activity Inferred from electronic annotation. Source: EC 4 iron, 4 sulfur cluster binding Inferred from electronic annotation. Source: UniProtKB-KW metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 380	380	3-isopropylmalate dehydratase large subunit 2 HAMAP MF_01027		PRO_0000076878
Sites
	Metal binding	262	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	320	1	Iron-sulfur (4Fe-4S) By similarity
	Metal binding	323	1	Iron-sulfur (4Fe-4S) By similarity

Sequences

	Sequence		Length	Mass (Da)
	Q9V1J0 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: B22EE1E6D8016FAD	FASTA	380	41,088
	10 20 30 40 50 60 MTLVGKLLNA KPGEAVIRKV DLVYAHDGTM PLIIEAFNRI FNEVRTRAYI FFDHVYPAPT 70 80 90 100 110 120 VKVANLHREI REFAKIHGIP VVEGKGISHQ LVVELGLAEE AKIIVGGDSH TPTLGALGVF 130 140 150 160 170 180 AVGMGATDVA IALGLGKIWL KVPESIAVLL DGSPREYIMA SDVMIHLITS LKDREMSYNA 190 200 210 220 230 240 IEFFNVPFSF DERLTLTNFS VEANAKTAII GEEYEGGGYS DEITIELDSL PPMVAKPFSP 250 260 270 280 290 300 ANGVSVEDVE GTKIDQVFIG SCTNGRFEQI KRAAEILDGE QVNVRTLVAP ASINVYRRMI 310 320 330 340 350 360 EEGLVRILID AGVVILPPGC GPCLGRHMGV AGDNEVILST TNRNFRGRMG SPKAEIYLAS 370 380 PVTAAVSALY GEITNPEGEL

References

[1]

"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi." Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P. Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: GE5 / Orsay.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AJ248284 Genomic DNA. Translation: CAB49359.1.
PIR	H75159.
RefSeq	NP_126128.1. NC_000868.1.
3D structure databases
ProteinModelPortal	Q9V1J0.
ModBase	Search...
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBPYRT00000002543; EBPYRP00000002474; EBPYRG00000002543.
GeneID	1495331.
GenomeReviews	Gene locus PYRAB04370 in contig AL096836_GR.
KEGG	pab:PAB0287.
NMPDR	fig|272844.1.peg.455.
Organism-specific databases
CMR	Search...
Phylogenomic databases
GeneTree	EBGT00050000022452.
HOGENOM	HBG330745.
OMA	VEVDQVM.
PhylomeDB	Q9V1J0.
ProtClustDB	PRK00402.
Enzyme and pathway databases
BioCyc	PABY272844:PAB0287-MONOMER.
Family and domain databases
HAMAP	MF_01027. LeuC_type2. [Tree]
InterPro	IPR015931. Acnase/IPM_dHydase_lsu_aba_1/3. IPR015937. Acoase/IPM_deHydtase. IPR001030. Acoase/IPM_deHydtase_lsu_aba. IPR015932. Aconitase/IPMdHydase_lsu_aba_2. IPR018136. Aconitase_4Fe-4S_BS. IPR011826. HAcnase/IPMdehydase_lsu_prok. IPR006251. Homoacnase/IPMdehydase_lsu. [Graphical view]
Gene3D	G3DSA:3.30.499.10. Acnase/IPM_dHydase_lsu_aba_1/3. 2 hits. G3DSA:3.40.1060.10. Aconitase/IPMdHydase_lsu_aba_2. 1 hit.
KO	K01703.
PANTHER	PTHR11670. Aconitase-like_core. 1 hit. PTHR11670:SF16. PTHR11670:SF16. 1 hit.
Pfam	PF00330. Aconitase. 2 hits. [Graphical view]
PRINTS	PR00415. ACONITASE.
SUPFAM	SSF53732. Aconitase_N. 1 hit.
TIGRFAMs	TIGR02086. IPMI_arch. 1 hit.
PROSITE	PS00450. ACONITASE_1. 1 hit. PS01244. ACONITASE_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

LEUC2_PYRAB

Accession

Primary (citable) accession number: Q9V1J0

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 26, 2002
Last sequence update:	May 1, 2000
Last modified:	December 14, 2011
This is version 76 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program